9F3B: Detyrosinated tubulin alpha-1B chain

Undecorated 13pf E254Q microtubule from recombinant human tubulin. Determined by electron microscopy at 3.6 Å resolution. Released 19 Mar 2025.

Method: Electron microscopy
Resolution: 3.6 Å
Organism: Homo sapiens
Chains: 12
Atoms: 41,106
Mol. weight: 618.62 kDa
Ligands: MG, GTP
Released: 19 Mar 2025

Explore 9F3B in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9F3B contains 279 α-helices and 258 β-strands across 12 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 23 helices, 15 β-strands

Element	Residues	Length	Sheet
β-strand	3-9	7	1
α-helix	10-27	18
α-helix	49-51	3
β-strand	53-55	3	2
α-helix	56	1
β-strand	61-63	3	2
β-strand	65-69	5	1
α-helix	73-80	8
β-strand	93-94	2	1
α-helix	103-104	2
α-helix	105-109	5
α-helix	111-113	3
α-helix	115-128	14
β-strand	132-138	7	1
α-helix	144-160	17
β-strand	165-169	5	1
α-helix	172-174	3
α-helix	183-194	12
β-strand	200-202	3	1
β-strand	203	1	3
α-helix	206-215	10
α-helix	224-243	20
β-strand	248	1	3
α-helix	252-259	8
β-strand	269	1	3
β-strand	272-273	2	3
α-helix	279-282	4
α-helix	288-296	9
α-helix	298-300	3
α-helix	307-309	3
β-strand	312-321	10	3
α-helix	325-337	13
β-strand	351-356	6	3
α-helix	358-361	4
β-strand	373-381	9	3
α-helix	383-399	17
α-helix	405-410	6
α-helix	415-436	22

Chain B: 21 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	3-9	7	4
α-helix	10-27	18
β-strand	30	1	5
β-strand	35	1	6
β-strand	36	1	5
α-helix	42-45	4
β-strand	51-53	3	7
α-helix	55-57	3
β-strand	58	1	6
β-strand	59-61	3	7
β-strand	63-67	5	4
α-helix	71-78	8
α-helix	87-89	3
β-strand	91-92	2	4
α-helix	102-104	3
α-helix	109-126	18
β-strand	130-138	9	4
α-helix	143-158	16
β-strand	163-169	7	4
α-helix	170-172	3
α-helix	182-194	13
β-strand	198-200	3	4
β-strand	202	1	4
α-helix	205-213	9
α-helix	222-241	20
β-strand	246	1	8
α-helix	250-257	8
β-strand	260	1	9
β-strand	263	1	9
β-strand	265-266	2	4
β-strand	268-271	4	10
α-helix	286-293	8
α-helix	305-307	3
β-strand	310-319	10	10
α-helix	323-336	14
α-helix	338-340	3
β-strand	341	1	10
β-strand	349-352	4	10
β-strand	353	1	8
α-helix	357-358	2
β-strand	363-371	9	10
α-helix	374-390	17
α-helix	396-399	4
α-helix	405-426	22

Chain C: 24 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	2-8	7	23
α-helix	10-28	19
α-helix	49-51	3
β-strand	53-55	3	24
β-strand	61-63	3	24
β-strand	65-67	3	23
β-strand	68-69	2	25
α-helix	72-80	9
β-strand	93-94	2	25
α-helix	105-109	5
α-helix	111-128	18
β-strand	131-138	8	23
α-helix	144-160	17
β-strand	165-169	5	23
α-helix	172-174	3
α-helix	183-194	12
β-strand	200-202	3	23
β-strand	203	1	26
α-helix	206-211	6
α-helix	212-216	5
α-helix	224-238	15
α-helix	240-243	4
β-strand	248	1	27
α-helix	252-258	7
β-strand	269-273	5	26
α-helix	279-281	3
α-helix	288-294	7
α-helix	298-300	3
α-helix	307-309	3
β-strand	312-314	3	28
β-strand	317-318	2	29
β-strand	320-321	2	30
α-helix	325-335	11
β-strand	343	1	28
β-strand	353-354	2	29
β-strand	355	1	27
α-helix	359-361	3
α-helix	369-370	2
β-strand	373-374	2	30
β-strand	375-379	5	26
β-strand	380-381	2	28
α-helix	382-384	3
α-helix	385-399	15
α-helix	405-409	5
α-helix	415-436	22

Chain D: 25 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	3-9	7	31
α-helix	10-27	18
β-strand	30	1	32
β-strand	35	1	33
β-strand	36	1	32
α-helix	42-45	4
β-strand	53	1	34
α-helix	55-57	3
β-strand	58	1	33
β-strand	59	1	34
β-strand	63-67	5	31
α-helix	71-77	7
α-helix	87-89	3
β-strand	90-92	3	31
α-helix	102	1
α-helix	103-107	5
α-helix	109-123	15
β-strand	130-136	7	31
α-helix	143-147	5
α-helix	148-158	11
β-strand	163-166	4	31
α-helix	182-192	11
β-strand	198-200	3	31
α-helix	205-209	5
α-helix	210-214	5
α-helix	222-237	16
β-strand	246	1	35
α-helix	250-256	7
β-strand	260	1	36
β-strand	263	1	36
β-strand	265-266	2	31
β-strand	267-271	5	37
α-helix	277-279	3
α-helix	286-294	9
α-helix	305-307	3
β-strand	310-317	8	37
α-helix	324-336	13
α-helix	338-340	3
β-strand	341	1	37
β-strand	349-352	4	37
β-strand	353	1	35
α-helix	357-358	2
β-strand	365-371	7	37
α-helix	374-390	17
α-helix	395-397	3
α-helix	399-401	3
α-helix	405-427	23

Chain E: 28 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	3-9	7	51
α-helix	10-27	18
α-helix	49-51	3
β-strand	53-55	3	52
α-helix	56	1
β-strand	61-63	3	52
β-strand	65-69	5	51
α-helix	72-80	9
β-strand	93-94	2	51
α-helix	105-109	5
α-helix	111-113	3
α-helix	115-128	14
β-strand	132-138	7	51
α-helix	145-149	5
α-helix	150-160	11
β-strand	165-169	5	51
β-strand	172	1	53
α-helix	173-174	2
α-helix	183-194	12
α-helix	195-197	3
β-strand	200-202	3	51
β-strand	203	1	54
β-strand	205	1	53
α-helix	206-211	6
α-helix	212-216	5
α-helix	224-238	15
α-helix	240-243	4
β-strand	248	1	55
α-helix	252-258	7
β-strand	269	1	54
β-strand	272-273	2	56
α-helix	279-281	3
α-helix	288-295	8
α-helix	298-300	3
α-helix	307-309	3
β-strand	312-314	3	57
β-strand	320-321	2	58
α-helix	325-337	13
β-strand	343	1	57
β-strand	355	1	55
α-helix	359-361	3
α-helix	369-370	2
β-strand	373-374	2	58
β-strand	375-376	2	56
β-strand	379	1	54
β-strand	380-381	2	57
α-helix	382-384	3
α-helix	385-399	15
α-helix	405-409	5
α-helix	415-436	22

Chain F: 22 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	3-9	7	59
α-helix	10-27	18
β-strand	30	1	60
β-strand	35	1	61
β-strand	36	1	60
α-helix	41-44	4
β-strand	51-53	3	62
α-helix	55-57	3
β-strand	58	1	61
β-strand	59-61	3	62
β-strand	63-67	5	59
α-helix	73-78	6
β-strand	91-92	2	59
α-helix	102-105	4
α-helix	109-123	15
β-strand	130-136	7	59
α-helix	146-158	13
β-strand	163-166	4	59
α-helix	170-172	3
α-helix	182-192	11
β-strand	198-200	3	59
α-helix	205-209	5
α-helix	210-214	5
α-helix	222-237	16
β-strand	246	1	63
α-helix	250-257	8
β-strand	265-266	2	59
β-strand	270-271	2	64
α-helix	277-279	3
α-helix	286-293	8
α-helix	305-307	3
β-strand	310-316	7	65
α-helix	323-336	14
α-helix	338-340	3
β-strand	341	1	65
β-strand	349-352	4	65
β-strand	353	1	63
α-helix	357-358	2
β-strand	365-366	2	64
β-strand	369-371	3	65
α-helix	374-390	17
α-helix	399-401	3
α-helix	405-424	20

Chain G: 21 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	3-9	7	11
α-helix	10-27	18
α-helix	49-51	3
β-strand	53-55	3	12
β-strand	61-63	3	12
β-strand	65-69	5	11
α-helix	73-79	7
β-strand	93-94	2	11
α-helix	105-109	5
α-helix	111-113	3
α-helix	115-128	14
β-strand	132-138	7	11
α-helix	148-160	13
β-strand	165-169	5	11
α-helix	172-174	3
α-helix	183-194	12
β-strand	200-202	3	11
β-strand	203	1	13
α-helix	206-215	10
α-helix	224-238	15
α-helix	240-243	4
β-strand	248	1	14
α-helix	252-259	8
β-strand	269-273	5	13
α-helix	280-283	4
α-helix	288-296	9
α-helix	298-300	3
α-helix	307-309	3
β-strand	312-314	3	15
β-strand	317-321	5	13
α-helix	325-337	13
β-strand	343	1	15
β-strand	355	1	14
β-strand	373-379	7	13
β-strand	380-381	2	15
α-helix	384-400	17
α-helix	405-409	5
α-helix	415-436	22

Chain I: 25 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	3-9	7	38
α-helix	10-27	18
α-helix	49-51	3
β-strand	53-55	3	39
α-helix	56	1
β-strand	61-63	3	39
β-strand	65-69	5	38
α-helix	73-80	8
β-strand	93-94	2	38
α-helix	103-104	2
α-helix	105-109	5
α-helix	111-113	3
α-helix	115-128	14
β-strand	132-138	7	38
α-helix	145-149	5
α-helix	150-160	11
β-strand	165-169	5	38
β-strand	172	1	40
α-helix	173-174	2
α-helix	183-194	12
β-strand	200-202	3	38
β-strand	203	1	41
β-strand	205	1	40
α-helix	206-215	10
α-helix	224-238	15
α-helix	252-259	8
β-strand	269	1	41
β-strand	271	1	42
β-strand	272-273	2	43
α-helix	288-296	9
α-helix	298-300	3
β-strand	301	1	42
α-helix	307-309	3
β-strand	312	1	44
β-strand	320-321	2	45
α-helix	325-336	12
β-strand	343	1	44
α-helix	362-363	2
β-strand	373-374	2	45
β-strand	375-376	2	43
β-strand	379	1	41
β-strand	381	1	44
α-helix	382-384	3
α-helix	385-400	16
α-helix	405-409	5
α-helix	415-434	20
α-helix	438-440	3

4 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Detyrosinated tubulin alpha-1B chain	A, C, E, G, I, K	protein	453	Homo sapiens	P68363 (AlphaFold model)
Tubulin beta-3 chain	B, D, F, N, P, R	protein	456	Homo sapiens	Q13509 (AlphaFold model)

Sequence of entity 1 (A, C, E, G, I, K), FASTA

>9F3B_1 Detyrosinated tubulin alpha-1B chain (chains A, C, E, G, I, K)
MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIHHHHHHGGGHHHFNTFDS
FNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHY
TIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLE
FSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLN
RLISQIVSSITASLRFDGALNVDLTQFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSV
AEITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRSIQFVDWCP
TGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWY
VGEGMEEGEFSEAREDMAALEKDYEEVGVDSVE

Sequence of entity 2 (B, D, F, N, P, R), FASTA

>9F3B_2 Tubulin beta-3 chain (chains B, D, F, N, P, R)
MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPSGNYVGDSDLQLERISVYYNEASSHKYV
PRAILVDLEPGTMDSVRSGAFGHLFRPDNFIFGQSGAGNNWAKGHYTEGAELVDSVLDVV
RKECENCDCLQGFQLTHSLGGGTGSGMGTLLISKVREEYPDRIMNTFSVVPSPKVSDTVV
EPYNATLSIHQLVENTDETYCIDNEALYDICFRTLKLATPTYGDLNHLVSATMSGVTTSL
RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTARGSQQYRALTVPELTQQMFDAKNMM
AACDPRHGRYLTVATVFRGRMSMKEVDEQMLAIQSKNSSYFVEWIPNNVKVAVCDIPPRG
LKMSSTFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVS
EYQQYQDATAEEEGEMYEDDEEESEAQGPKENLYFQ

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	12
GTP	Guanosine-5'-triphosphate	C10 H16 N5 O14 P3	12

Primary citation

Hydrolysis-deficient mosaic microtubules as faithful mimics of the GTP cap. Estevez-Gallego, J., Blum, T.B., Ruhnow, F. et al. Nat Commun (2025) 16:2396-2396. DOI 10.1038/s41467-025-57555-6 · PubMed

Other PDB entries of the same protein (UniProt P68363 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6S8L 1.8 Å, Structure, Thermodynamics, and Kinetics of Plinabulin Binding to two Tubulin Isotypes
6J8O 1.85 Å, Structure of a hypothetical protease
7PJF 1.86 Å, Inhibiting parasite proliferation using a rationally designed anti-tubulin agent
6J4V 2.1 Å, Structural basis of tubulin detyrosination by vasohibins-SVBP enzyme complex and…
8VT7 2.66 Å, Structure of the gamma tubulin ring complex nucleated microtubule protofilament.
7Z6S 2.9 Å, MATCAP bound to a human 14 protofilament microtubule
8V2J 2.9 Å, Structure of alpha1B and betaI/IVb microtubule bound to GDP
9COC 2.9 Å, Two protofilament structure of alpha1B and betaI/IVb microtubule bound to GDP
9BP6 3.1 Å, Structure of alpha1B and betaI/IVb microtubule bound to GMPCPP
9CMM 3.1 Å, Two protofilament structure of alpha1B and betaI/IVb microtubule bound to GMPCPP
7LXB 3.26 Å, HeLa-tubulin in complex with cryptophycin 52
9HQ4 3.28 Å, TTLL11 bound to microtubule

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